Striated ciliary root-golgi association in branchial crown epithelial cells ofOwenia. Visualization of Ca2+-binding sites and ATPase activities

PROTOPLASMA ◽  
1986 ◽  
Vol 130 (2-3) ◽  
pp. 108-119 ◽  
Author(s):  
J. Coulon ◽  
J. P. Arsanto ◽  
Y. Thouveny
Keyword(s):  
Epithelial Cells ◽  
Binding Sites ◽  
Branchial Crown

Progastrin1–80stimulates growth of intestinal epithelial cells in vitro via high-affinity binding sites

2003 ◽  
Vol 284 (2) ◽  
pp. G328-G339 ◽  
Author(s):  
P. Singh ◽  
X. Lu ◽  
S. Cobb ◽  
B. T. Miller ◽  
N. Tarasova ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Binding Sites ◽  
Intestinal Epithelial Cells ◽  
Full Length ◽  
Intestinal Epithelial ◽  
Growth Effects ◽  
High Affinity ◽  
Significant Difference

Proliferation and carcinogenesis of the large intestinal epithelial cells (IEC) cells is significantly increased in transgenic mice that overexpress the precursor progastrin (PG) peptide. It is not known if the in vivo growth effects of PG on IEC cells are mediated directly or indirectly. Full-length recombinant human PG (rhPG1–80) was generated to examine possible direct effects of PG on IEC cells. Surprisingly, rhPG (0.1–1.0 nM) was more effective than the completely processed gastrin 17 (G17) peptide as a growth factor. Even though IEC cells did not express CCK1and CCK2receptors (-R), fluorescently labeled G17 and Gly-extended G17 (G-Gly) were specifically bound to the cells, suggesting the presence of binding proteins other than CCK1-R and CCK2-R on IEC cells. High-affinity ( Kd= 0.5–1.0 nM) binding sites for125I-rhPG were discovered on IEC cells that demonstrated relative binding affinity for gastrin-like peptides in the order PG ≥ COOH-terminally extended G17 ≥ G-Gly > G17 > *CCK-8 (* significant difference; P< 0.05). In conclusion, our studies demonstrate for the first time direct growth effects of the full-length precursor peptide on IEC cells in vitro that are apparently mediated by the high-affinity PG binding sites that were discovered on these cells.

Specific binding sites for growth hormone in cultured mouse thymic epithelial cells

Life Sciences ◽  
1991 ◽  
Vol 48 (22) ◽  
pp. 2141-2148 ◽  
Author(s):  
Elisabeth Ban ◽  
Marie-Claude Gagnerault ◽  
Hélène Jammes ◽  
Marie-Catherine Postel-Vinay ◽  
France Haour ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Epithelial Cells ◽  
Binding Sites ◽  
Specific Binding ◽  
Thymic Epithelial Cells ◽  
Specific Binding Sites

196 EPITHELIAL–MESENCHYMAL TRANSITION IN EQUINE AMNIOTIC PROGENITOR CELLS INDUCES CHANGES OF THE CELL GLYCAN PROFILE

2014 ◽  
Vol 26 (1) ◽  
pp. 212
Author(s):  
A. Lange-Consiglio ◽  
G. Accogli ◽  
F. Cremonesi ◽  
S. Desantis
Keyword(s):  
Epithelial Cells ◽  
Progenitor Cells ◽  
Binding Sites ◽  
Epithelial Mesenchymal Transition ◽  
Lectin Binding ◽  
Mesenchymal Transition ◽  
Glycan Profile ◽  
Amniotic Epithelial Cells

Epithelial to mesenchymal transition (EMT) is the process by which epithelial cells dramatically alter their shape and motile behaviour as they differentiate into mesenchymal cells. The EMT and the reverse process, termed mesenchymal–epithelial transition, play central roles in embryogenesis. Gastrulation and neural crest formation are processes governed by EMT in amniotes. It is noteworthy that in placental mammals, the epithelial layer of amnion originates from the trophectoderm and it is continuous with the epiblast. On this basis, it is reasonable to speculate that some amniotic epithelial cells may escape the specification that accompanies gastrulation, and may retain some of the characteristics of epiblastic cells, such as pluripotency, behaving as stem cells that are able to preserve intrinsically the ability to transdifferentiate. Because it seems that malignant cells use the same mechanisms during the formation of tumours in vivo, the amniotic epithelial cells (AEC) could represent a good model to study in vitro this phenomenon that we observed to occur spontaneously in our culture conditions. The aim of this study was to characterise the glycoprotein pattern expressed in fresh or cryopreserved equine AEC, mesenchymal (AMC), and transdifferentiated cells by means of lectin histochemistry. AEC and AMC were cultured until passage (P) 3, while transdifferentiated cells at P1(EMT1) and P2 (EMT2). All cell lines were frozen for 1 month at –196°C in liquid nitrogen. The glycoanalysis was performed with a panel of twelve lectins to detect the glycans terminating with sialic acids (MAL II, SNA, PNA after sialidase digestion (K-s), K-s-DBA), galactose (PNA, RCA120, GSA I-B4,), N-acetylgalactosamine (DBA, HPA, SBA), N-acetylglucosamine (GSA II), fucose (UEA I, LTA), or with internal mannose (Con A). After freezing: 1) AEC exhibited decrease of binding sites for DBA, SBA, HPA, GSA II, and disappearance of GSA I-B4 and UEA I binders; 2) AMC displayed increase of SBA reactivity, decrease of K-s-PNA, HPA, GSA II staining, and absence of GSA I-B4 affinity; 3) EMT1 cells showed the appearance of K-s-DBA staining, the increase of K-s-PNA, RCA120, SBA, GSA I-B4, and UEA I reactivity, the decrease of MAL II, SNA, HPA, GSA II binders, and the disappearance of DBA and LTA binding sites; 4) EMT2 cells revealed the increase of K-s-PNA, GSA I-B4, UEA I affinity, the decrease of MAL II, SNA, RCA120, HPA, GSA II binders, and the lack of DBA, SBA, and LTA reactivity. In conclusion, this study demonstrates that the EMT induces changes in cell surface glycan profile of equine amniotic progenitor cells, and for the first time revealed that freezing modifies the lectin binding pattern of these cells. The observed glycan pattern modification may represent one aspect of the spontaneous complex process of EMT.

Specific binding of endothelin-1 to canine tracheal epithelial cells in culture

1995 ◽  
Vol 268 (3) ◽  
pp. L424-L431 ◽  
Author(s):  
H. Ninomiya ◽  
X. Y. Yu ◽  
Y. Uchida ◽  
S. Hasegawa ◽  
E. W. Spannhake
Keyword(s):  
Epithelial Cells ◽  
Binding Site ◽  
Binding Sites ◽  
Specific Binding ◽  
Receptor Subtype ◽  
Control Mechanisms ◽  
Endothelin 1 ◽  
Tracheal Epithelial Cells ◽  
Eta Receptor ◽  
Tracheal Epithelial

We have studied the binding of endothelin-1 (ET-1) to cultured canine tracheal epithelial cells. A single specific binding site for 125I-labeled ET-1 was identified with an apparent dissociation constant (Kd) of 0.2 nM, maximal binding sites (Bmax) of 6.7 x 10(3) sites/cell, and half-maximal inhibition (IC50) of 0.3 nM during a 2-h incubation period. The binding of 125I-ET-1 to these cells was inhibited by the presence of unlabeled ET-1, ET-2, or BQ-123, whereas ET-3 and sarafotoxin S6c did not compete for this binding site. These binding characteristics are consistent with those of the ETA receptor. At 37 degrees C, specific binding continuously increased over 18 h, while at 4 degrees C, it reached a plateau by 2 h. The increase in binding at 37 degrees C was not associated with DNA synthesis but was dependent upon protein synthesis, suggesting that epithelial binding sites were produced continuously under these incubation conditions. Our results indicate that canine tracheal epithelial cells possess specific binding sites for ET-1 with characteristics similar to those of the ETA receptor subtype. Because these cells are demonstrated to both release and bind ET-1, the results further suggest that ET-1 is involved in paracrine and/or autocrine control mechanisms in the airway epithelium.

scholarly journals Lectin-binding sites in epithelial cells of the mouse prostate gland

2015 ◽  
Vol 91 (4) ◽  
pp. 91-95 ◽  
Author(s):  
Kentaro SAKUDA ◽  
Ayaka YOSHIDA ◽  
Ryoki MURAGISHI ◽  
Kazuya YOSHINAGA
Keyword(s):  
Epithelial Cells ◽  
Binding Sites ◽  
Lectin Binding ◽  
Prostate Gland ◽  
Mouse Prostate ◽  
Lectin Binding Sites

Identification of α2-adrenoceptors and non-adrenergic idazoxan binding sites in rabbit colon epithelial cells

1990 ◽  
Vol 191 (1) ◽  
pp. 59-68 ◽  
Author(s):  
Jean Michel Senard ◽  
Dominique Langin ◽  
Luis Estan ◽  
Hervé Paris
Keyword(s):  
Epithelial Cells ◽  
Binding Sites ◽  
Α2 Adrenoceptors ◽  
Rabbit Colon

Identification of cholera toxin-binding sites in the nucleus of intestinal epithelial cells

FEBS Letters ◽  
1989 ◽  
Vol 242 (2) ◽  
pp. 309-313 ◽  
Author(s):  
Marianne E. Parkinson ◽  
Colin G. Smith ◽  
Peter B. Garland ◽  
Simon van Heyningen
Keyword(s):  
Epithelial Cells ◽  
Cholera Toxin ◽  
Binding Sites ◽  
Intestinal Epithelial Cells ◽  
Intestinal Epithelial ◽  
Toxin Binding

scholarly journals Two barium binding sites on a maxi K+ channel from human vas deferens epithelial cells

1996 ◽  
Vol 70 (3) ◽  
pp. 1316-1325 ◽  
Author(s):  
Y. Sohma ◽  
A. Harris ◽  
C.J. Wardle ◽  
B.E. Argent ◽  
M.A. Gray
Keyword(s):  
Epithelial Cells ◽  
Binding Sites ◽  
Vas Deferens ◽  
K Channel
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